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The expression of heat shock protein in human skeletal muscle: effects of muscle fibre phenotype and training background
Örebro universitet, Institutionen för hälsovetenskap och medicin. (Muscle & Exercise Physiology Research Group (MEP-RG) , RISPA)
Department of Orthopaedic Surgery M, Faculty of Health Sciences, Institute of Sports Medicine, Bispebjerg Hospital, Copenhagen, Denmark; Centre for Healthy Ageing, University of Copenhagen, Copenhagen, Denmark.
Department of Orthopaedic Surgery M, Faculty of Health Sciences, Institute of Sports Medicine, Bispebjerg Hospital, Copenhagen, Denmark; Centre for Healthy Ageing, University of Copenhagen, Copenhagen, Denmark.
Örebro universitet, Institutionen för hälsovetenskap och medicin.
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2013 (Engelska)Ingår i: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 209, nr 1, s. 26-33Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Aim: Exercise-induced adaptations of skeletal muscle are related to training mode and can be muscle fibre type specific. This study aimed to investigate heat shock protein expression in type I and type II muscle fibres in resting skeletal muscle of subjects with different training backgrounds.

Methods: Three groups of subjects were included: healthy active not engaged in any training programme (ACT, n = 12), resistance trained (RES, n = 6) and endurance trained (END, n = 8). Biopsies were obtained from vastus lateralis, and immunohistochemistry was performed using monoclonal antibodies against myosin heavy chain I and IIA, αB-crystallin, HSP27, HSP60 and HSP70.

Results: In ACT and RES, but not in END, a fibre type–specific expression with higher staining intensity in type I than type II fibres was seen for αB-crystallin. The opposite (II > I) was found for HSP27 in subjects from ACT (6 of 12 subjects) and RES (3 of 6), whereas all subjects from END displayed uniform staining. HSP60 showed no fibre-specific expression. HSP70 displayed a fibre-specific expression pattern (I > II) in ACT (4 of 12), but not in END or RES.

Conclusion: This study shows that the level of expression of the different HSPs in human skeletal muscle is influenced by muscle fibre phenotype. The fibre type–specific expression of HSP70 is influenced by resistance and endurance training, whereas those of αB-crystallin and HSP27 is influenced only by endurance training, suggesting the existence of a training-modality-specific action on the adaptive processes including heat shock proteins in human skeletal muscle.

Ort, förlag, år, upplaga, sidor
Wiley-Blackwell, 2013. Vol. 209, nr 1, s. 26-33
Nyckelord [en]
Adaptation, endurance, heat shock protein, immunohistochemistry, resistance
Nationell ämneskategori
Idrottsvetenskap
Forskningsämne
Idrott med inriktning mot fysiologi
Identifikatorer
URN: urn:nbn:se:oru:diva-30127DOI: 10.1111/apha.12124ISI: 000322950400006PubMedID: 23710799Scopus ID: 2-s2.0-84881557932OAI: oai:DiVA.org:oru-30127DiVA, id: diva2:639130
Anmärkning

Funding agency:

Nordea Foundation

Tillgänglig från: 2013-08-06 Skapad: 2013-08-06 Senast uppdaterad: 2018-11-19Bibliografiskt granskad
Ingår i avhandling
1. Heat shock proteins in exercised human skeletal muscle
Öppna denna publikation i ny flik eller fönster >>Heat shock proteins in exercised human skeletal muscle
2018 (Engelska)Doktorsavhandling, sammanläggning (Övrigt vetenskapligt)
Abstract [en]

Exercise is considered as an important stressor accompanied by concerted molecular and cellular changes leading to adaptations at the level of skeletal muscle size and function. An important protein family produced by cells in response to stressful conditions is the heat shock proteins (HSPs). It is suggested that the different HSPs play specific roles in acute and longterm responses to exercise-induced stress. The overall aim of this thesis was to explore the expression of four different HSPs (αB-crystallin, HSP27, HSP60 and HSP70) in human skeletal muscle exposed to exercise, with a special emphasis on the role played by HSP27 in the hypertrophy of human skeletal muscle.

One of the major findings was the fibre type-specific expression of HSPs in resting human skeletal muscle, including the preferential expression of HSP27 in fast type II muscle fibres. Another finding was the occurrence of training background-related differences in the expression of HSPs. Also, a cytoplasmic relocation of HSP27, occurring specifically in type II muscle fibres, was shown in response to a single bout of resistance exercise. Interestingly, there were no corresponding changes in response to an endurance exercise bout, suggesting that HSP27 may be specifically involved in the adaptations to resistance exercise. In order to test this hypothesis, an in-vitro exercise model based on the electrical pulse stimulation (EPS) of muscle cells was developed. The EPS protocol, including an 8 h restitution period, induced a significant hypertrophy of muscle cells together with molecular changes similar to those previously described in response to exercise in humans. The role of HSP27 in the hypertrophy of human muscle cells was examined through the downregulation of HSP27. Based on data from morphological and microarray analyses, findings indicate that HSP27 is not mandatory for the hypertrophy of human muscle cells. Overall, the present thesis clarified the expression of different HSPs in human skeletal muscle and provided an in-vitro-based approach for the elucidation of the exact role played by HSPs in the adaptations of human skeletal muscle to exercise.

Ort, förlag, år, upplaga, sidor
Örebro: Örebro University, 2018. s. 56
Serie
Örebro Studies in Sport Sciences, ISSN 1654-7535 ; 28
Nyckelord
Endurance training, Resistance training, Muscle Fibre Type, Electrical Pulse Stimulation, Muscle Hypertrophy
Nationell ämneskategori
Idrottsvetenskap
Identifikatorer
urn:nbn:se:oru:diva-68028 (URN)978-91-7529-260-1 (ISBN)
Disputation
2018-10-17, Örebro universitet, Gymnastik- och idrottshuset, Hörsal G, Fakultetsgatan 1, Örebro, 09:00 (Engelska)
Opponent
Handledare
Tillgänglig från: 2018-07-23 Skapad: 2018-07-23 Senast uppdaterad: 2018-09-25Bibliografiskt granskad

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